Tag | Content |
---|
CPLM ID | CPLM-016020 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Formin-binding protein 1 |
Protein Synonyms/Alias | Formin-binding protein 17 |
Gene Name | Fnbp1 |
Gene Synonyms/Alias | Fbp17; Kiaa0554 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
---|
166 | DADINVTKADVEKAR | ubiquitination | [1] | 319 | FGGKSRGKLWPFIKK | ubiquitination | [1] | 377 | FNEFMTSKPKIHCFR | ubiquitination | [1] | 456 | DPASLDQKLTEVTQN | ubiquitination | [1] | 611 | YVEVYLDKNAKGS** | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May act as a link between RND2 signaling and regulation of the actin cytoskeleton. May be required for the lysosomal retention of FASLG/FASL (By similarity). |
Sequence Annotation | DOMAIN 1 65 FCH. REPEAT 415 490 REM. DOMAIN 549 610 SH3. REGION 1 334 Interaction with microtubules (By REGION 1 288 F-BAR domain (By similarity). REGION 1 79 Required for self-association and REGION 251 616 Required for self-association and REGION 399 551 Interaction with RND2 (By similarity). REGION 494 616 Interaction with PDE6G (By similarity). REGION 513 616 Required for interaction with TNKS (By REGION 534 616 Interaction with DNM1 and DNM3 (By REGION 549 616 Interaction with ARHGAP17, DAAM1, DIAPH1 REGION 552 609 Interaction with FASLG (By similarity). REGION 552 608 Interaction with DNM2 and WASL (By MOD_RES 66 66 N6-acetyllysine (By similarity). MOD_RES 110 110 N6-acetyllysine (By similarity). MOD_RES 294 294 Phosphothreonine. MOD_RES 296 296 Phosphoserine. MOD_RES 299 299 Phosphoserine. MOD_RES 348 348 Phosphoserine (By similarity). MOD_RES 358 358 Phosphoserine (By similarity). MOD_RES 496 496 Phosphoserine. MOD_RES 499 499 Phosphotyrosine. |
Keyword | Acetylation; Alternative splicing; Cell membrane; Coated pit; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Lipid-binding; Lysosome; Membrane; Phosphoprotein; Reference proteome; SH3 domain. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 616 AA |
Protein Sequence | MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK 60 EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV DLMRYVQELK QERKSNFHDG 120 RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRQ 180 QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ 240 VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL 300 SSSKEGKPEL RFGGKSRGKL WPFIKKNKLM SLLTSPHQPP PPPPASASPS AVPNGPQSPK 360 QPKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED FSNFPPEQRR KKLQQKVDDL 420 NREIQKETDQ RDAITKMKDV YLKNPQMGDP ASLDQKLTEV TQNIEKLRLE AQKFEAWLAE 480 VEGRLPARSE QARRQSGLYD GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLAPDFDD 540 EFDDEEPLPA IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV 600 PTSYVEVYLD KNAKGS 616 |
Gene Ontology | GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. GO:0005905; C:coated pit; IEA:UniProtKB-SubCell. GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell. GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0008289; F:lipid binding; IEA:UniProtKB-KW. GO:0006897; P:endocytosis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |